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The Journal of Experimental Biology 206, 399-409 (2003)
doi: 10.1242/jeb.00074

Expression and localization of carbonic anhydrase and ATPases in the symbiotic tubeworm Riftia pachyptila

Marie-Cécile De Cian^*, Ann C. Andersen, Xavier Bailly and François H. Lallier

Equipe Ecophysiologie, CNRS-UPMC UMR 7127 CEOBM, Station Biologique, BP 74, F-29682 Roscoff Cedex, France

^* Author for correspondence (e-mail: decian{at}sb-roscoff.fr)

Accepted 14 October 2002

The symbiotic tubeworm Riftia pachyptila needs to fuel its chemoautotrophic symbiotic bacteria with inorganic carbon. CO₂ is transported from the surrounding water to the bacteriocytes located in the trophosome, through the branchial plume and the body fluids. Previous studies have demonstrated the implication of carbonic anhydrase (CA) and proton pumps (ATPases) at various steps of CO₂ transport. The present study describes the expression pattern of cytosolic CA using an RNA probe and its histochemical and immunocytochemical localization in the trophosome and branchial plume of Riftia. Immunolocalization of V-H⁺ATPase and Na⁺K⁺-ATPase were also performed and related to CA localization. In the branchial plume, CA is expressed and localized in the most apical region of the branchial epithelium, close to the surrounding water. V-H⁺ATPase is mostly colocalized with CA and both enzymes probably allow CO₂ entry against the concentration gradient while regulating intracellular pH. Na⁺K⁺-ATPase is mostly restricted to the basal part of epithelial cells and probably participates in CO₂ transport to the body fluids. In the trophosome lobules, cytosolic CA is expressed and found in bacteriocytes and peritoneal cells. Hypotheses on the role of CA in bicarbonate and CO₂ interconversion to fuel the symbiotic bacteria are discussed.

Key words: Vestimentifera, carbonic anhydrase, V-H⁺ATPase, Na⁺K⁺-ATPase, immunolocalization, in situ hybridization

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